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Structure of K. pneumonia mrkh in its apo state.

Analyse Structure of K. pneumonia mrkh in its apo state. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KEC
Type
protein
Length
454 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flagellar brake protein ycgr
UniProt
G3FT00
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
DFlagellar brake protein ycgrprotein22217% helix, 49% strandG3FT00
AFlagellar brake protein ycgrprotein23217% helix, 49% strandG3FT00

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18440.750.7963empty
25850.700.7969empty
31150.470.7919empty
41180.380.7519empty
5540.280.7512empty

Interfaces

1 interface between chains.

  • D–A · 2208 Ų buried · 52 hydrogen bonds · protein-protein

Compared structures

  • 5KEC · Structure of K. pneumonia MrkH in its apo state. · the same entry in another collection · chain D against D, TM-score 1.00

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